Purification and characterization of a high-molecular-weight insecticidal protein complex produced by the entomopathogenic bacterium photorhabdus luminescens /

QR-koodi

Purification and characterization of a high-molecular-weight insecticidal protein complex produced by the entomopathogenic bacterium photorhabdus luminescens /

Tallennettuna:

Bibliografiset tiedot
Päätekijä:	Bowen, David J.
Muut tekijät:	Ensign, Jerald C.
Aineistotyyppi:	Artikkeli
Kieli:	English
Aiheet:	Biological activity Characterization Entomopathogen Microbial insecticides Protein Purification Toxin
Tagit:	Lisää tagi Ei tageja, Lisää ensimmäinen tagi!

Thư viện lưu trữ:	Thư viện Trường Đại học Đà Lạt

Samankaltaisia teoksia

A novel insecticidal toxin from photorhabdus luminescens, toxin complex a (Tca), its histopathological effects on the midgut of manduca sexta /

Biochemical and molecular characterization of the insecticidal fragment of CryV /

Photobactin : A catechol siderophore produced by photorhabdus luminescens, an entomopathogen mutually associated with heterorhabditis bacteriophora NC1 nematodes /

Composition and biophysical properties of lipids in xenorhabdus nematophilus and photorhabdus luminescens, symbiotic bacteria associated with entomopathogenic nematodes /

Cloning and characterization of a cytolytic and mosquitocidal delta- endotoxin from Bacillus thuringiensis subsp. Jegathesan /
Tekijä: Cheong, H.

In vitro and in vivo characterization of a small-colony variant of the primary form of photorhabdus luminescens MD (Enterobacteriaceae) /
Tekijä: Hu, Kaiji.

Isolation, purification, characterization of the PR oxidase from penicillium roqueforti /

Insecticidal activity of bacillus laterosporus /

Identification and characterization of a previously undescribed cyt gene in Bacillus thuringiensis subsp. israelensis /
Tekijä: Guerchicoff, A.

Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium rhodococcus ruber DSM 44541 /
Tekijä: Pogorevc, Mateja.

Purification and characterization of streptin, a type A1 lantibiotic produced by streptococcus pyogenes /
Tekijä: Wescombe, Philip A.

The mode of action of the bacillus thuringiensis vegetative insecticidal protein vip3A differs from that of cry1ab delta-endotoxin /

The introduction into bacillus sphaericus of the bacillus thuringiensis subsp. medellin cyt1Ab1 Gene results in higher susceptibility of resistant mosquito larva populations to B. sphaericus /

Interactions of insecticidal toxin gene products from xenorhabdus nematophilus PMFI296 /

Purification and characterization of a novel bacteriocin produced by enterococcus faecalis strain RJ-11 /

Activities of bacillus thuringiensis insecticidal crystal proteins Cyt1Aa and Cyt2Aa against three species of sheep blowfly /

A holistic approach for determining the entomopathogenic potential of bacillus thuringiensis strains /

Comparison of the cellular fatty acid composition of a bacterium isolated from a human and alleged to be Bacillus sphaericus with that of Bacillus sphaericus isolated from a mosquito larvicide /
Tekijä: Siegel, J. P.

Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium /
Tekijä: Wang, S. L.

Purification and characterization of alpha-L-arabinopyranosidase and -L-arabinofuranosidase from bifidobacterium breve K-110, a human intestinal anaerobic bacterium metabolizing ginsenoside Rb2 and Rc /

Purification and characterization of a novel erythrose reductase from Candida magnoliae /

Purification and characterization of laccase from chaetomium thermophilium and its role in humification /
Tekijä: Chefetz, Benny.

Purification, characterization, nucleotide sequence of an intracellular maltotriose-producing alpha-amylase from Streptococcus bovis 148 /

GTP cyclohydrolase I : Purification, characterization, effects of inhibition on nitric oxide synthase in nocardia species /
Tekijä: He, Aimin.

Modern insecticides and world food production
Tekijä: F A Gunther
Julkaistu: (1960)

Cyt1Aa protein of bacillus thuringiensis is toxic to the cottonwood leaf beetle, chrysomela scripta, and suppresses high levels of resistance to Cry3Aa /
Tekijä: Federici, Brian A.

Purification and characterization of an nad-malic enzyme from bradyrhizobium japonicum A1017 /

Purification and characterization of a trehalose synthase from the basidiomycete grifola frondosa /

Molecular cloning and characterization of a novel mosquitocidal protein gene from Bacillus thuringiensis subsp. fukuokaensis /
Tekijä: Lee, H. K.

Effects of midgut-protein-preparative and ligand binding procedures on the toxin binding characteristics of BT-R1, a common high-affinity receptor in manduca sexta for Cry1A bacillus thuringiensis toxins /

Unique regulation of crystal protein production in Bacillus thuringiensis subsp. yunnanensis is mediated by the cry protein- encoding 103-megadalton plasmid /

Insecticide action: from molecule to organism
Julkaistu: (1989)

Purification and characterization of a nylon-degrading enzyme /

Purification and characterization of a proteasome from the hyperthermophilic archaeon pyrococcus furiosus /
Tekijä: Bauer, M. W.

Purification and characterization of a novel mannitol dehydrogenase from a newly isolated strain of Candida magnoliae /

Microbial utilization of free and clay-bound insecticidal toxins from bacillus thuringiensis and their retention of insecticidal activity after incubation with microbes /
Tekijä: Koskella, J.

The Bacillus thuringiensis vegetative insecticidal protein Vip3A lyses midgut epithelium cells of susceptible insects /

Gene cloning, purification, characterization of a phosphodiesterase from delftia acidovorans /
Tekijä: Tehara, Sundiep K.

Phage display of a biologically active bacillus thuringiensis toxin /

Influence of exposure to single versus multiple toxins of bacillus thuringiensis subsp. israelensis on development of resistance in the mosquito culex quinquefasciatus (Diptera : Culicidae) /
Tekijä: Georghiou, G. P.